4 research outputs found
Engineering Stability-Tunable DNA Micelles Using Photocontrollable Dissociation of an Intermolecular G‑Quadruplex
Because
of their facile preparation, small size (<100 nm), programmable
design, and biocompatibility, lipid-based DNA micelles show enormous
potential as a tool to monitor biological events and treat human diseases.
However, their structural stability in biological matrices suffers
from spatiotemporal variability, thus limiting their <i>in vivo</i> use. Herein, we have engineered stability-tunable DNA micelle flares
using photocontrollable dissociation of intermolecular G-quadruplexes,
which confers DNA micelle flares with robust structural stability
against disruption by serum albumin. However, once exposed to light,
the G-quadruplex formation is blocked by strand hybridization, resulting
in the loss of stability in the presence of serum albumin and subsequent
cellular uptake. This programmable regulation to stabilize lipid-based
micelles in the presence of fatty-acid-binding serum albumin should
further the development of biocompatible DNA micelles for <i>in vivo</i> applications
Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer
Identifying missing proteins (MPs)
has been one of the critical
missions of the Chromosome-Centric Human Proteome Project (C-HPP).
Since 2012, over 30 research teams from 17 countries have been trying
to search adequate and accurate evidence of MPs through various biochemical
strategies. MPs mainly fall into the following classes: (1) low-molecular-weight
(LMW) proteins, (2) membrane proteins, (3) proteins that contained
various post-translational modifications (PTMs), (4) nucleic acid-associated
proteins, (5) low abundance, and (6) unexpressed genes. In this study,
kidney cancer and adjacent tissues were used for phosphoproteomics
research, and 8962 proteins were identified, including 6415 phosphoproteins,
and 44 728 phosphosites, of which 10 266 were unreported
previously. In total, 75 candidate detections were found, including
45 phoshoproteins. GO analysis for these 75 candidate detections revealed
that these proteins mainly clustered as membrane proteins and took
part in nephron and kidney development. After rigorous screening and
manual check, 9 of them were verified with the synthesized peptides.
Finally, only one missing protein was confirmed. All mass spectrometry
data from this study have been deposited in the PRIDE with identifier
PXD006482
Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer
Identifying missing proteins (MPs)
has been one of the critical
missions of the Chromosome-Centric Human Proteome Project (C-HPP).
Since 2012, over 30 research teams from 17 countries have been trying
to search adequate and accurate evidence of MPs through various biochemical
strategies. MPs mainly fall into the following classes: (1) low-molecular-weight
(LMW) proteins, (2) membrane proteins, (3) proteins that contained
various post-translational modifications (PTMs), (4) nucleic acid-associated
proteins, (5) low abundance, and (6) unexpressed genes. In this study,
kidney cancer and adjacent tissues were used for phosphoproteomics
research, and 8962 proteins were identified, including 6415 phosphoproteins,
and 44 728 phosphosites, of which 10 266 were unreported
previously. In total, 75 candidate detections were found, including
45 phoshoproteins. GO analysis for these 75 candidate detections revealed
that these proteins mainly clustered as membrane proteins and took
part in nephron and kidney development. After rigorous screening and
manual check, 9 of them were verified with the synthesized peptides.
Finally, only one missing protein was confirmed. All mass spectrometry
data from this study have been deposited in the PRIDE with identifier
PXD006482
Deep Coverage Proteomics Identifies More Low-Abundance Missing Proteins in Human Testis Tissue with Q‑Exactive HF Mass Spectrometer
Since 2012, missing proteins (MPs)
investigation has been one of
the critical missions of Chromosome-Centric Human Proteome Project
(C-HPP) through various biochemical strategies. On the basis of our
previous testis MPs study, faster scanning and higher resolution mass-spectrometry-based
proteomics might be conducive to MPs exploration, especially for low-abundance
proteins. In this study, Q-Exactive HF (HF) was used to survey proteins
from the same testis tissues separated by two separating methods (tricine-
and glycine-SDS-PAGE), as previously described. A total of 8526 proteins
were identified, of which more low-abundance proteins were uniquely
detected in HF data but not in our previous LTQ Orbitrap Velos (Velos)
reanalysis data. Further transcriptomics analysis showed that these
uniquely identified proteins by HF also had lower expression at the
mRNA level. Of the 81 total identified MPs, 74 and 39 proteins were
listed as MPs in HF and Velos data sets, respectively. Among the above
MPs, 47 proteins (43 neXtProt PE2 and 4 PE3) were ranked as confirmed
MPs after verifying with the stringent spectra match and isobaric
and single amino acid variants filtering. Functional investigation
of these 47 MPs revealed that 11 MPs were testis-specific proteins
and 7 MPs were involved in spermatogenesis process. Therefore, we
concluded that higher scanning speed and resolution of HF might be
factors for improving the low-abundance MP identification in future
C-HPP studies. All mass-spectrometry data from this study have been
deposited in the ProteomeXchange with identifier PXD004092